Identification of a New Broadly Cross-reactive Epitope within Domain III of the Duck Tembusu Virus E Protein

Autor: Ming Liu, Ronghong Hua, Qingshan Zhang, Wulin Shaozhou, Jyung-Hurng Liu, Chenxi Li, Runze Meng, Yun Zhang, Xiaofei Bai
Rok vydání: 2016
Předmět:
Zdroj: Scientific Reports
ISSN: 2045-2322
DOI: 10.1038/srep36288
Popis: In 2010, a pathogenic flavivirus termed duck Tembusu virus (DTMUV) caused widespread outbreak of egg-drop syndrome in domesticated ducks in China. Although the glycoprotein E of DTMUV is an important structural component of the virus, the B-cell epitopes of this protein remains uncharacterized. Using phage display and mutagenesis, we identified a minimal B-cell epitope, 374EXE/DPPFG380, that mediates binding to a nonneutralizing monoclonal antibody. DTMUV-positive duck serum reacted with the epitope, and amino acid substitutions revealed the specific amino acids that are essential for antibody binding. Dot-blot assays of various flavivirus-positive sera indicated that EXE/DPPFG is a cross-reactive epitope in most flaviviruses, including Zika, West Nile, Yellow fever, dengue, and Japanese encephalitis viruses. These findings indicate that the epitope sequence is conserved among many strains of mosquito-borne flavivirus. Protein structure modeling revealed that the epitope is located in domain III of the DTMUV E protein. Together, these results provide new insights on the broad cross-reactivity of a B-cell binding site of the E protein of flaviviruses, which can be exploited as a diagnostic or therapeutic target for identifying, studying, or treating DTMUV and other flavivirus infections.
Databáze: OpenAIRE